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Journals
Toxins
Special Issues
Pore-Forming Toxins from Feature to Function
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Pore-Forming Toxins from Feature to Function

A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Bacterial Toxins".

Deadline for manuscript submissions: closed (29 February 2024) | Viewed by 1969

Special Issue Editors

Dr. Brad Spicer

E-Mail Website
Guest Editor
Monash Biomedicine Discovery Institute (BDI), Department of Biochemistry and Molecular Biology, Monash University, Level 2, 23 Innovation Walk (Building 77), Clayton VIC 3800, Australia
Interests: pore forming proteins
Dr. Hannah L Best

E-Mail Website
Guest Editor
School of Biosciences, Cardiff University, Park Place, Cardiff CF10 3AX, UK
Interests: neuroscience; molecular biology; ecology
Prof. Dr. Colin Berry

E-Mail Website
Guest Editor
School of Biosciences, Cardiff University, Museum Avenue, Cardiff CF10 3AX, UK
Interests: invertebrate-active toxins; protein toxins; biological control; protein structure-function

Special Issue Information

Dear Colleagues,

Pore-forming proteins have been instrumental in the development of new biotechnology. These pore-forming biotechnologies have a wide breadth of applications, including as agricultural crop protectants, nanopores for sequencing, and as tools for stopping the spread of vector-borne diseases. Furthermore, there are many families of pore-forming proteins such as Cry, App, aerolysin, MACPF/CDC and others, each of which performs its function in a unique manner. Indeed, the many unique features of pore-forming proteins (e.g., receptor binding, oligomerization, and membrane insertion) lend themselves to having a tunable function that can be exploited in the development of biotechnology.

The focus of this Special Issue of Toxins will be on pore-forming proteins across all families with the potential for novel applications. This may include pore-forming proteins with insecticidal properties, biotechnology such as sequencing or other pore-related discoveries. We welcome articles/reviews with new insights or perspectives on pore-forming proteins. This includes new structural or mechanistic insights, mutational analyses, and works defining novel applications for these proteins.

Dr. Brad Spicer
Dr. Hannah L Best
Prof. Dr. Colin Berry
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a double-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Toxins is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • pore-forming proteins
  • biotechnology
  • insecticidal
  • receptor binding
  • molecular mechanism
  • oligomerization

Published Papers (1 paper)

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Research

18 pages, 8575 KiB  
Article
Structural Basis of Clostridium perfringens Enterotoxin Activation and Oligomerization by Trypsin
by Chinemerem P. Ogbu, Srajan Kapoor and Alex J. Vecchio
Toxins 2023, 15(11), 637; https://doi.org/10.3390/toxins15110637 - 31 Oct 2023
Viewed by 1507
Abstract
Clostridium perfringens enterotoxin (CpE) is a β-pore forming toxin that disrupts gastrointestinal homeostasis in mammals by binding membrane protein receptors called claudins. Although structures of CpE fragments bound to claudins have been determined, the mechanisms that trigger CpE activation and oligomerization that lead [...] Read more.
Clostridium perfringens enterotoxin (CpE) is a β-pore forming toxin that disrupts gastrointestinal homeostasis in mammals by binding membrane protein receptors called claudins. Although structures of CpE fragments bound to claudins have been determined, the mechanisms that trigger CpE activation and oligomerization that lead to the formation of cytotoxic β-pores remain undetermined. Proteolysis of CpE in the gut by trypsin has been shown to play a role in this and subsequent cytotoxicity processes. Here, we report solution structures of full-length and trypsinized CpE using small-angle X-ray scattering (SAXS) and crystal structures of trypsinized CpE and its C-terminal claudin-binding domain (cCpE) using X-ray crystallography. Mass spectrometry and SAXS uncover that removal of the CpE N-terminus by trypsin alters the CpE structure to expose areas that are normally unexposed. Crystal structures of trypsinized CpE and cCpE reveal unique dimer interfaces that could serve as oligomerization sites. Moreover, comparisons of these structures to existing ones predict the functional implications of oligomerization in the contexts of cell receptor binding and β-pore formation. This study sheds light on trypsin’s role in altering CpE structure to activate its function via inducing oligomerization on its path toward cytotoxic β-pore formation. Its findings can incite new approaches to inhibit CpE-based cytotoxicity with oligomer-disrupting therapeutics. Full article
(This article belongs to the Special Issue Pore-Forming Toxins from Feature to Function)
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